2fjs
From Proteopedia
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|PDB= 2fjs |SIZE=350|CAPTION= <scene name='initialview01'>2fjs</scene>, resolution 1.85Å | |PDB= 2fjs |SIZE=350|CAPTION= <scene name='initialview01'>2fjs</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span> |
|GENE= nirK, nir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis]) | |GENE= nirK, nir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1aq8|1AQ8]], [[1as7|1AS7]], [[1as8|1AS8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjs OCA], [http://www.ebi.ac.uk/pdbsum/2fjs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fjs RCSB]</span> | ||
}} | }} | ||
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[[Category: Murphy, M E.P.]] | [[Category: Murphy, M E.P.]] | ||
[[Category: Tocheva, E I.]] | [[Category: Tocheva, E I.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: CU1]] | ||
| - | [[Category: TRS]] | ||
[[Category: blue copper protein]] | [[Category: blue copper protein]] | ||
[[Category: cupredoxin fold]] | [[Category: cupredoxin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:03:45 2008'' |
Revision as of 00:03, 31 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | nirK, nir (Alcaligenes faecalis) | ||||||
| Activity: | Nitrite reductase (NO-forming), with EC number 1.7.2.1 | ||||||
| Related: | 1AQ8, 1AS7, 1AS8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Anaerobically Reduced Wild Type Nitrite Reductase from A. faecalis
Overview
Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. The former acts as the electron acceptor site of the enzyme, and the latter is the site of catalytic action. The effect of the methionine ligand on the reorganization energy of the type-1 site was explored by studying the electron-transfer kinetics between NiR (wild type (wt) and the variants Met150Gly and Met150Thr) with Fe(II)EDTA and Fe(II)HEDTA. The mutations increased the reorganization energy by 0.3 eV (30 kJ mol-1). A similar increase was found from pulse radiolysis experiments on the wt NIR and three variants (Met150Gly, Met150His, and Met150Thr). Binding of the nearby Met62 to the type-1 Cu site in Met150Gly (under influence of an allosteric effector) lowered the reorganization energy back to approximately the wt value. According to XRD data the structure of the reduced type-1 site in Met150Gly NiR in the presence of an allosteric effector is similar to that in the reduced wt NiR (solved to 1.85 A), compatible with the similarity in reorganization energy.
About this Structure
2FJS is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.
Reference
Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase., Wijma HJ, MacPherson I, Farver O, Tocheva EI, Pecht I, Verbeet MP, Murphy ME, Canters GW, J Am Chem Soc. 2007 Jan 24;129(3):519-25. PMID:17227014
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